› 6gi5

X-ray diffraction
3.11Å resolution

Crystal structure of the ferric enterobactin esterase (PfeE) from Pseudomonas aeruginosa in complex with the tris-catechol vector

Released:
DOI: 10.2210/pdb6gi5/pdb
PDB entry 6gi5 coloured by chain, front view.
PDB entry 6gi5 coloured by chain, side view.
PDB entry 6gi5 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
A Key Role for the Periplasmic PfeE Esterase in Iron Acquisition via the Siderophore Enterobactin in Pseudomonas aeruginosa.
Perraud Q, Moynié L, Gasser V, Munier M, Godet J, Hoegy F, Mély Y, Mislin GLA, Naismith JH, Schalk IJ
ACS Chem Biol 13 2603-2614 (2018)
PMID: 30086222

Function and Biology Details

Reaction catalysed: 
(1a) iron(III)-enterobactin + H(2)O = iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine trimer  complex
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191234 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Iron(III) enterobactin esterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 282 amino acids
Theoretical weight: 30.65 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I0F2 (Residues: 27-304; Coverage: 100%)
Gene names: PA2689, pfeE
Sequence domains: Putative esterase

Ligands and Environments

2 bound ligands:
Ligand FE 2 x FE
Ligand 8SW 2 x 8SW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: I4122
Unit cell:
a: 126.612Å b: 126.612Å c: 293.711Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.242 0.285
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Engineering Siderophore Biosynthesis and Regulation Pathways to Increase Diversity and Availability.
Puja et al. (2023)
1 more

1 mention without citation

Parsing the functional specificity of Siderocalin/Lipocalin 2/NGAL for siderophores and related small-molecule ligands.
Clifton et al. (2019)